ID W9WKT8_9EURO Unreviewed; 1655 AA.
AC W9WKT8;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Adenosinetriphosphatase {ECO:0000313|EMBL:EXJ65610.1};
GN ORFNames=A1O5_11137 {ECO:0000313|EMBL:EXJ65610.1};
OS Cladophialophora psammophila CBS 110553.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=1182543 {ECO:0000313|EMBL:EXJ65610.1, ECO:0000313|Proteomes:UP000019471};
RN [1] {ECO:0000313|EMBL:EXJ65610.1, ECO:0000313|Proteomes:UP000019471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 110553 {ECO:0000313|EMBL:EXJ65610.1,
RC ECO:0000313|Proteomes:UP000019471};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Cladophialophora psammophila CBS 110553.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Component of the SWR1 chromatin-remodeling complex.
CC {ECO:0000256|ARBA:ARBA00011826}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. SWR1 subfamily.
CC {ECO:0000256|ARBA:ARBA00009220}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EXJ65610.1}.
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DR EMBL; AMGX01000024; EXJ65610.1; -; Genomic_DNA.
DR RefSeq; XP_007749900.1; XM_007751710.1.
DR STRING; 1182543.W9WKT8; -.
DR GeneID; 19195827; -.
DR eggNOG; KOG0391; Eukaryota.
DR HOGENOM; CLU_000315_24_2_1; -.
DR OrthoDB; 5475375at2759; -.
DR Proteomes; UP000019471; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.20.120.850; SWI2/SNF2 ATPases, N-terminal domain; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014012; HSA_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45685:SF1; HELICASE SRCAP; 1.
DR PANTHER; PTHR45685; HELICASE SRCAP-RELATED; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07529; HSA; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51204; HSA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000019471}.
FT DOMAIN 360..434
FT /note="HSA"
FT /evidence="ECO:0000259|PROSITE:PS51204"
FT DOMAIN 792..957
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1346..1496
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 489..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 632..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 718..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1555..1608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1628..1655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..184
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..531
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..548
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..609
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..755
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1637..1655
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1655 AA; 188436 MW; 5327922B0B0E22CF CRC64;
MPIPSPTGDF QSDSNTQHQD LLNKRSTSPI RNQESPVRSS VDPHDGHDGP PAKRRKVAGT
DHKSSPRLIS PPWKRVVAEG PASFIQDGRR KSGRTNIVPL DLQPQSNKRQ TRAAFDKAKE
ERQKHAKPVY NVSARKSKIE AHVSPPVTVK RGPVPPSKGH DVSQSQHHRK AEASQRHLRD
TILISKHPHL TQPKSPRHRT SAHRDTVITS THPHSTQPKS PRHRASAAHR PQTTPPRLSV
AYGDKPQTNG IVKIEQESDD DNLDTSSGLS SRGSTPPVTL RKVTFRVRLP PPSVASPANV
PLPKKYASFE EFLEKDETEP RTGEETLTRD QVEKEAVARQ RVKDAQKRGS LHNKFVDALP
DKQDEPGRQY AHRDHLLAHV CHFRNLLRAE HREHKRKAEI LAHEAKRYVE KKQKRNKVKT
AEEIEQEKRE ACVAIYRTVV KDIDKLWAAV RQEVNAIRQK EYEEQQQAKM KGHLARVLDR
TDQMLTRLAE QDDSMMDSET DLSSNETTES ESENSEQMSE SETETESEPD DGDHDAQMSI
EELKKKYGNL PDLPIAHEGP FSDGKAEDEE SLDQPDAESD PETEMDSEFD TSGSGDEDEG
EEGESEEDET GGGLLSMLFS KKQIVDMTLE ADEMDASKKE ESESRNNLLV QVLEDVPIPK
AEPSEADRTP VQNGQEKLKA EATSEHSVQL EAPTAQETDN AGLRDATPLI HSQIARLPSE
DPGSQEHSSH PSPHTTTTKF SEPGSLSSID VRTGSVPPVT PSEAKSVIKT PVPSLLRGTL
REYQHEGLDW LADLYAHGRS GILADEMGLG KTIQSIALLA HLAEVYEVWG PHLIVVPTSV
MLNWEMEFKK FLPGFKVLTY YGNLEERKQK RRGWMADDSF NVCITSYQLV LQDANSFKRR
KWHYMILDEA HNIKNFRSER WQTMMTFNTR ARLLLTGTPL QNNLTELWSL LFFLHYGQEN
EGEDDAFAGL KEWSEWFKRP VESILEHGRQ ALDEEDREQV AKLHKVIRPF LLRRLKADVE
KQMPAKYEHV EMCRLSKRQR QLYDGFMSRA QTKETLASGN YLSIINALMQ LRKVCNHPDL
FETRPINTSF AMHKSAAADF EIKDFLVRRR LMLDASNNLD LDFLRLVPIS EERLSMIEVI
ETTKRHAYNQ LRDLREAQSR RVLSSSRNSI HNDNATSWRG ETRRGVLGSL ENVGRRARLQ
ELDRTMYYEA YKHHQHPIYG CGLIDQLTIN TTYERLSKLS PRRVLSRLWD EDQPMRSLNL
IHSVQSRSGQ MQPFVDKYAC VTPAVVATDL YARTVTEAGA QAIREAAEST LKRDDEDDPF
HLARMKLSIA FPDKRLLQYD CGKLQRLDKL LRQLQAGSHR ALIFTQMTKV LDILEQFLNI
HGHRYLRLDG ATKIEQRQIL TERFNNDTRI LCFILSSRSG GLGINLTGAD TVIFYDLDWN
PAMDKQCTDR AHRIGQTRDV HIYRFVSEHT IESNILRKAN QKQMLDDVVI QEGDFTTDYM
NRMTYRDMLD ENAEEDEAGK AMDRVLGNEN SSIKELEQAE DQEDRVAAKV AARELQHADE
GDFEDGRASA TPRTQTGDAR STPASGVVPG EPFGATDTAI TQPQDEEERI HHIDEYLIQL
QRYLMKDIPL GPGKDSKKGK KGRRGRDEHR VRRVR
//
